Exposure of luminal membranes of LLC-PK1 cells to ANG II induces dimerization of AT(1)/AT(2) receptors to activate SERCA and to promote Ca2+ mobilization [PDF]
, 2012 Ferrao FM, Lara LS, Axelband F, Dias J, Carmona AK, Reis RI, Costa-Neto CM, Vieyra A, Lowe J. Exposure of luminal membranes of LLC-PK1 cells to ANG II induces dimerization of AT(1)/AT(2) receptors to activate SERCA and to promote Ca2+ mobilization.
Axelband, Flavia +8 more
core +1 more source
Amyloid beta and Alzheimer’s Disease: The role of neprilysin-2 in amyloid-beta clearance
Frontiers in Aging Neuroscience, 2014 Accumulation of the amyloid-beta (Ab) peptide is a central factor in Alzheimer’s disease (AD) pathogenesis as supported by continuing evidence. This review concisely summarizes this evidence supporting a critical role for Ab in AD before discussing the ...
Robert eMarr, Daniel eHafez
doaj +1 more source
Amyloid-Beta Protein Clearance and Degradation (ABCD) Pathways and their Role in Alzheimer’s Disease [PDF]
, 2015 Amyloid-β proteins (Aβ) of 42 (Aβ42) and 40 aa (Aβ40) accumulate as senile plaques (SP) and cerebrovascular amyloid protein deposits that are defining diagnostic features of Alzheimer's disease (AD). A number of rare mutations linked to familial AD (FAD)
Baranello, Robert J. +7 more
core +1 more source
Phosphorylation-deficient G-protein-biased μ-opioid receptors improve analgesia and diminish tolerance but worsen opioid side effects [PDF]
, 2019 Opioid analgesics are powerful pain relievers; however, over time, pain control diminishes as analgesic tolerance develops. The molecular mechanisms initiating tolerance have remained unresolved to date.
Bailey, A +8 more
core +2 more sources
Aging Cell, Volume 19, Issue 11, November 2020., 2020 AICD‐mediated regulatory feedback cycle of IDE and APP processing. Abstract One of the major pathological hallmarks of Alzheimer´s disease (AD) is an accumulation of amyloid‐β (Aβ) in brain tissue leading to formation of toxic oligomers and senile plaques.
Anna A. Lauer +13 more
wiley +1 more source
The use of Fluorescence Resonance Energy Transfer (FRET) peptidesfor measurement of clinically important proteolytic enzymes [PDF]
, 2009 Proteolytic enzymes have a fundamental role in many biological processes and are associated with multiple pathological conditions. Therefore, targeting these enzymes may be important for a better understanding of their function and development of ...
Carmona, Adriana Karaoglanovic +2 more
core +3 more sources
The FASEB Journal, Volume 34, Issue 9, Page 12922-12931, September 2020., 2020 Abstract Pleiotropic roles are proposed for brain extracellular vesicles (EVs) in the development of Alzheimer's disease (AD). Our previous studies have suggested a beneficial role for EVs in AD, where the endosomal system in vulnerable neurons is compromised, contributing to the removal of accumulated material from neurons. However, the involvement of
Rocío Pérez‐González +5 more
wiley +1 more source
Neurodegeneration-Associated Protein Fragments as Short-Lived Substrates of the N-End Rule Pathway [PDF]
, 2013 Protein aggregates are a common feature of neurodegenerative syndromes. Specific protein fragments were found to be aggregated in disorders including Alzheimer’s disease, amyotrophic lateral sclerosis, and Parkinson’s disease.
Brower, Christopher S. +2 more
core +2 more sources
Effect of hyperglycemia and rosiglitazone on renal and urinary neprilysin in db/db diabetic mice
Physiological Reports, Volume 8, Issue 3, February 2020., 2020 Decreased intrarenal NEP, which could have a pivotal role in the pathogenesis of diabetic kidney disease. Urinary NEP could be an index of intra‐renal NEP status. The renoprotective effects of rosiglitazone could be mediated by the up‐regulation of renal NEP expression and activity in db/db diabetic mice. Abstract Alteration in renin‐angiotensin system
Laale F. Alawi +6 more
wiley +1 more source
Bradykinin Release Avoids High Molecular Weight Kininogen Endocytosis [PDF]
, 2015 Human H-kininogen (120 kDa) plays a role in many pathophysiological processes and interacts with the cell surface through protein receptors and proteoglycans, which mediate H-kininogen endocytosis.
Araujo, Mariana S. +9 more
core +3 more sources